Kinetics of Binding of Multisubstrate Analogue Inhibitor (2-Amino-9-[2-(Phosphonomethoxy)Ethyl]-6-Sulfanylpurine) with Trimeric Purine Nucleoside Phosphorylase |
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| Authors: | Jan Antosiewicz Beata Wielgus-Kutrowska Maciej D?ugosz Antonin Holy Agnieszka Bzowska |
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| Institution: | 1. Department of Biophysics , Institute of Experimental Physics, Warsaw University , Warsaw , Poland;2. Institute of Organic Chemistry and Biochemistry &3. Centre for Novel Antivirals and Antineoplastics, Flemingeve nam. 2 , Czech Republic |
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| Abstract: | Complex formation of multisubstrate analogue inhibitor—2-amino-9-2-(phosphonomethoxy)ethyl]-6-sulfanylpurine (PME-6-thio-Gua) with trimeric purine nucleoside phosphorylase from Cellulomonas sp. was investigated using a stopped-flow spectrofluorimetric approach. Results obtained indicate that, in contrast to binding of guanine, i.e., the transition-state conformation trapping ligand, for which binding at each active site is followed by the enzyme conformational change, association of the ground-state analogue PME-6-thio-Gua is a one-step process. |
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| Keywords: | Binding PME-6-thio-Gua multisubstrate analogue inhibitor |
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